シグナル伝達とCa^<++>要求性リン脂質結合蛋白 : 特にリポコルチン様蛋白について
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概要
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Ca^<2+> acts as an intracellular second messenger by virtue of its concentrationdependent binding to regulatory proteins. In the cell, all intracellular Ca^<2+>-binding proteins were thought to belong to single structural group, characterized by the presence of an EF hand structure. However, recently it has characterized the intracellular Ca^<2+>-dependent lipid-binding protein as a distinct family by several properties including immunologically cross-reaction. This new family protein is involved in metabolic regulation in the cell by Ca^<2+> and phospholipid. Protein Kinase C, Ca^<2+>-dependent protease (CANP/Calpain), and lipocortin (carpactin) are the typical proteins of the family. During the course of study on the mechanism of superoxide generation in guinea pig neutrophils, we found a large amount of Ca^<2+>-dependent phospholipdbinding 33 KDa protein (p33). The protein has a quite similar properties with that of lipocortin I obtained from human placenta . In this paper, the author described the outline of lipocortin like protein and the biological and biochemical properties of the p33. The 33 KDa proteis has following several properties ; 1) association with liposomal membrane containing acidic phospholipids in Ca^<2+> dependent manner, 2) distribution only in neutrophils, 3) inhibition of the phospholipase A_2,4) binding with actin, 5) phosphorylation by protein Kinase C (on serine residue), 6) similar component of amino acid with that of other lipocortin-like proteins, and 7) homologous amino acid sequence with human lipocortin l. These results indicate that the p33 plays an important roles in signal transduction system of neutrophil.
- 高知大学の論文
- 1988-12-10
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- シグナル伝達とCa^要求性リン脂質結合蛋白 : 特にリポコルチン様蛋白について